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3BDY.pdb
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HEADER HORMONE 15-NOV-07 3BDY
TITLE DUAL SPECIFIC BH1 FAB IN COMPLEX WITH VEGF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB FRAGMENT -HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB FRAGMENT -LIGHT CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR A;
COMPND 11 CHAIN: V;
COMPND 12 FRAGMENT: SEQUENCE DATABASE RESIDUES 27-135;
COMPND 13 SYNONYM: VEGF-A, VASCULAR PERMEABILITY FACTOR, VPF;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: VEGF, VEGFA;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FAB COMPLEX, ANGIOGENESIS, DEVELOPMENTAL PROTEIN, DIFFERENTIATION,
KEYWDS 2 GLYCOPROTEIN, GROWTH FACTOR, HEPARIN-BINDING, MITOGEN, SECRETED,
KEYWDS 3 HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.BOSTROM,C.WIESMANN,B.A.APPLETON
REVDAT 4 13-JUL-11 3BDY 1 VERSN
REVDAT 3 31-MAR-09 3BDY 1 JRNL
REVDAT 2 24-FEB-09 3BDY 1 VERSN
REVDAT 1 18-NOV-08 3BDY 0
JRNL AUTH J.BOSTROM,S.F.YU,D.KAN,B.A.APPLETON,C.V.LEE,K.BILLECI,W.MAN,
JRNL AUTH 2 F.PEALE,S.ROSS,C.WIESMANN,G.FUH
JRNL TITL VARIANTS OF THE ANTIBODY HERCEPTIN THAT INTERACT WITH HER2
JRNL TITL 2 AND VEGF AT THE ANTIGEN BINDING SITE
JRNL REF SCIENCE V. 323 1610 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19299620
JRNL DOI 10.1126/SCIENCE.1165480
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24225
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1248
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1340
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4072
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.01000
REMARK 3 B22 (A**2) : -0.56000
REMARK 3 B33 (A**2) : 1.58000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.410
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.283
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.206
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4184 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2829 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5688 ; 1.255 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6899 ; 0.805 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 524 ; 6.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;37.833 ;24.220
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 674 ;15.219 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;15.435 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 624 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4644 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 826 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 607 ; 0.185 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2648 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1943 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2298 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 98 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.346 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.140 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.075 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3373 ; 2.769 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1063 ; 0.517 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4260 ; 3.645 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1871 ; 2.670 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1428 ; 3.823 ; 5.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 0 H 115
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4998 -52.3042 1.7867
REMARK 3 T TENSOR
REMARK 3 T11: -0.2637 T22: -0.1109
REMARK 3 T33: -0.2229 T12: -0.0369
REMARK 3 T13: -0.0034 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 3.8860 L22: 3.7232
REMARK 3 L33: 2.0411 L12: 0.6662
REMARK 3 L13: 1.1764 L23: -0.3963
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: -0.2249 S13: 0.1224
REMARK 3 S21: 0.1727 S22: -0.0860 S23: 0.0037
REMARK 3 S31: -0.0941 S32: 0.1319 S33: 0.0773
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 116 H 215
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5629 -27.6691 6.8947
REMARK 3 T TENSOR
REMARK 3 T11: 0.2365 T22: 0.0986
REMARK 3 T33: -0.1399 T12: 0.0188
REMARK 3 T13: -0.0386 T23: -0.1095
REMARK 3 L TENSOR
REMARK 3 L11: 8.8573 L22: 4.8558
REMARK 3 L33: 2.6832 L12: 0.0200
REMARK 3 L13: 0.3558 L23: 0.1268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0486 S12: -1.3177 S13: 0.1570
REMARK 3 S21: 0.9493 S22: 0.0889 S23: -0.1741
REMARK 3 S31: -0.3100 S32: -0.4198 S33: -0.0403
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 109
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4596 -58.8465 -10.6603
REMARK 3 T TENSOR
REMARK 3 T11: -0.2283 T22: -0.1765
REMARK 3 T33: -0.2066 T12: -0.0530
REMARK 3 T13: 0.0169 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 4.4846 L22: 1.2973
REMARK 3 L33: 1.4973 L12: -0.8890
REMARK 3 L13: 1.1810 L23: -0.3277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: 0.1869 S13: -0.1329
REMARK 3 S21: -0.0295 S22: 0.0113 S23: 0.0392
REMARK 3 S31: 0.0637 S32: -0.0473 S33: -0.0200
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 110 L 213
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8848 -21.8276 -6.5557
REMARK 3 T TENSOR
REMARK 3 T11: 0.1654 T22: -0.0806
REMARK 3 T33: 0.0534 T12: 0.0607
REMARK 3 T13: 0.0316 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 5.7254 L22: 6.7518
REMARK 3 L33: 2.6788 L12: 2.7456
REMARK 3 L13: 1.2566 L23: 0.7894
REMARK 3 S TENSOR
REMARK 3 S11: -0.4113 S12: 0.2746 S13: 1.0980
REMARK 3 S21: 0.2808 S22: 0.3532 S23: 0.2070
REMARK 3 S31: -0.9660 S32: -0.1375 S33: 0.0581
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 14 V 108
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1874 -95.9046 -7.6920
REMARK 3 T TENSOR
REMARK 3 T11: 0.3551 T22: -0.0513
REMARK 3 T33: 0.2601 T12: 0.0473
REMARK 3 T13: -0.0175 T23: -0.0999
REMARK 3 L TENSOR
REMARK 3 L11: 0.3596 L22: 9.1840
REMARK 3 L33: 1.1560 L12: 0.8805
REMARK 3 L13: -0.4052 L23: -3.2093
REMARK 3 S TENSOR
REMARK 3 S11: -0.1310 S12: 0.0398 S13: -0.1964
REMARK 3 S21: -1.3429 S22: 0.0132 S23: -0.0483
REMARK 3 S31: 0.6267 S32: 0.0130 S33: 0.1178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3BDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-07.
REMARK 100 THE RCSB ID CODE IS RCSB045399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24705
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1N8Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: FOR CRYSTALLIZATION OF THE FAB/VEGF
REMARK 280 (8-109) COMPLEX, EQUAL VOLUMES OF PROTEIN COMPLEX SOLUTION (10.6
REMARK 280 MG/ML PROTEIN, 300 MM NACL, 25 MM TRIS-HCL PH 7.5) AND
REMARK 280 CRYSTALLIZATION BUFFER CONTAINING 0.15 D, L MALIC ACID PH 7.0,
REMARK 280 20% PEG3350 WERE MIXED AND EQUILIBRATED AT 19 C. PRIOR TO DATA
REMARK 280 COLLECTION THE CRYSTALS WERE CRYO-PROTECTED BY TRANSFER BETWEEN
REMARK 280 DROPS CONTAINING 5%, 10% AND 15% GLYCEROL IN ARTIFICIAL MOTHER
REMARK 280 LIQUOR, FOLLOWED BY FLASH FREEZE IN LIQUID NITROGEN, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.82500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.82500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 50.30000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 98.98900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.30000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 98.98900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.82500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.30000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 98.98900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.82500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.30000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 98.98900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -197.97800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU H -2
REMARK 465 ILE H -1
REMARK 465 LYS H 131
REMARK 465 SER H 132
REMARK 465 THR H 133
REMARK 465 SER H 134
REMARK 465 GLY H 135
REMARK 465 LYS H 216
REMARK 465 SER H 217
REMARK 465 CYS H 218
REMARK 465 ASP H 219
REMARK 465 LYS H 220
REMARK 465 THR H 221
REMARK 465 HIS H 222
REMARK 465 CYS L 214
REMARK 465 GLY V 8
REMARK 465 GLN V 9
REMARK 465 ASN V 10
REMARK 465 HIS V 11
REMARK 465 HIS V 12
REMARK 465 GLU V 13
REMARK 465 ASP V 109
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS H 92 CB CYS H 92 SG -0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN H 206 47.44 38.00
REMARK 500 SER L 77 86.71 -156.47
REMARK 500 ALA L 84 171.19 175.36
REMARK 500 ASN L 138 72.61 53.30
REMARK 500 ASN L 152 -11.55 73.18
REMARK 500 LYS L 190 -64.38 -103.41
REMARK 500 ARG L 211 93.79 -67.68
REMARK 500 CYS V 26 104.67 -18.95
REMARK 500 GLU V 42 81.21 -62.08
REMARK 500 GLN V 87 -57.34 -127.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BE1 RELATED DB: PDB
DBREF 3BDY H -2 222 PDB 3BDY 3BDY 1 230
DBREF 3BDY L 1 214 PDB 3BDY 3BDY 1 218
DBREF 3BDY V 8 109 UNP P15692 VEGFA_HUMAN 34 135
SEQRES 1 H 230 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY
SEQRES 2 H 230 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 H 230 ALA SER GLY PHE ASN ILE LYS ASP THR TYR ILE HIS TRP
SEQRES 4 H 230 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA
SEQRES 5 H 230 ARG ILE TYR PRO THR ASN GLY TYR THR ARG TYR ALA ASP
SEQRES 6 H 230 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER
SEQRES 7 H 230 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA
SEQRES 8 H 230 GLU ASP THR ALA VAL TYR TYR CYS SER ARG TRP GLY GLY
SEQRES 9 H 230 ASP GLY PHE TYR ALA MET ASP TYR TRP GLY GLN GLY THR
SEQRES 10 H 230 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 H 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 H 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 H 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 H 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 H 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 H 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 H 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 H 230 GLU PRO LYS SER CYS ASP LYS THR HIS
SEQRES 1 L 218 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 218 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 218 GLN ASP ILE PRO ARG SER ILE SER GLY TYR VAL ALA TRP
SEQRES 4 L 218 TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE
SEQRES 5 L 218 TYR TRP GLY SER TYR LEU TYR SER GLY VAL PRO SER ARG
SEQRES 6 L 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR
SEQRES 7 L 218 ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR
SEQRES 8 L 218 CYS GLN GLN HIS TYR THR THR PRO PRO THR PHE GLY GLN
SEQRES 9 L 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO
SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS
SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE
SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN
SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU
SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR
SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL
SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO
SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 V 102 GLY GLN ASN HIS HIS GLU VAL VAL LYS PHE MET ASP VAL
SEQRES 2 V 102 TYR GLN ARG SER TYR CYS HIS PRO ILE GLU THR LEU VAL
SEQRES 3 V 102 ASP ILE PHE GLN GLU TYR PRO ASP GLU ILE GLU TYR ILE
SEQRES 4 V 102 PHE LYS PRO SER CYS VAL PRO LEU MET ARG CYS GLY GLY
SEQRES 5 V 102 CYS CYS ASN ASP GLU GLY LEU GLU CYS VAL PRO THR GLU
SEQRES 6 V 102 GLU SER ASN ILE THR MET GLN ILE MET ARG ILE LYS PRO
SEQRES 7 V 102 HIS GLN GLY GLN HIS ILE GLY GLU MET SER PHE LEU GLN
SEQRES 8 V 102 HIS ASN LYS CYS GLU CYS ARG PRO LYS LYS ASP
HET GOL L 215 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *47(H2 O)
HELIX 1 1 ASN H 28 THR H 32 5 5
HELIX 2 2 ARG H 83 THR H 87 5 5
HELIX 3 3 SER H 158 ALA H 160 5 3
HELIX 4 4 SER H 189 LEU H 191 5 3
HELIX 5 5 LYS H 203 ASN H 206 5 4
HELIX 6 6 GLN L 79 PHE L 83 5 5
HELIX 7 7 SER L 121 LYS L 126 1 6
HELIX 8 8 LYS L 183 LYS L 188 1 6
HELIX 9 9 LYS V 16 SER V 24 1 9
HELIX 10 10 ILE V 35 TYR V 39 1 5
SHEET 1 A 4 GLN H 3 SER H 7 0
SHEET 2 A 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 A 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18
SHEET 4 A 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81
SHEET 1 B 6 GLY H 10 VAL H 12 0
SHEET 2 B 6 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 B 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 109
SHEET 4 B 6 ILE H 34 GLN H 39 -1 N HIS H 35 O SER H 93
SHEET 5 B 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 B 6 THR H 57 TYR H 59 -1 O ARG H 58 N ARG H 50
SHEET 1 C 4 GLY H 10 VAL H 12 0
SHEET 2 C 4 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 C 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 109
SHEET 4 C 4 TYR H 104 TRP H 105 -1 O TYR H 104 N ARG H 94
SHEET 1 D 4 SER H 122 LEU H 126 0
SHEET 2 D 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 D 4 TYR H 178 PRO H 187 -1 O VAL H 186 N ALA H 138
SHEET 4 D 4 VAL H 165 THR H 167 -1 N HIS H 166 O VAL H 183
SHEET 1 E 4 SER H 122 LEU H 126 0
SHEET 2 E 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 E 4 TYR H 178 PRO H 187 -1 O VAL H 186 N ALA H 138
SHEET 4 E 4 VAL H 171 LEU H 172 -1 N VAL H 171 O SER H 179
SHEET 1 F 3 THR H 153 TRP H 156 0
SHEET 2 F 3 TYR H 196 HIS H 202 -1 O ASN H 199 N SER H 155
SHEET 3 F 3 THR H 207 VAL H 213 -1 O THR H 207 N HIS H 202
SHEET 1 G 4 MET L 4 SER L 7 0
SHEET 2 G 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 G 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19
SHEET 4 G 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 H 6 SER L 10 SER L 14 0
SHEET 2 H 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 H 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 H 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 H 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 H 6 TYR L 53 LEU L 54 -1 O TYR L 53 N TYR L 49
SHEET 1 I 4 SER L 10 SER L 14 0
SHEET 2 I 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 I 4 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 I 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 J 4 ILE L 29 SER L 30 0
SHEET 2 J 4 GLY V 88 PRO V 106 -1 O ILE V 91 N SER L 30
SHEET 3 J 4 LEU V 66 LYS V 84 -1 N ILE V 76 O PHE V 96
SHEET 4 J 4 ILE V 46 LYS V 48 -1 N ILE V 46 O ILE V 83
SHEET 1 K 4 SER L 114 PHE L 118 0
SHEET 2 K 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114
SHEET 3 K 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132
SHEET 4 K 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 L 4 ALA L 153 LEU L 154 0
SHEET 2 L 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 L 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 L 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SHEET 1 M 2 HIS V 27 ASP V 34 0
SHEET 2 M 2 CYS V 51 GLY V 58 -1 O LEU V 54 N THR V 31
SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.00
SSBOND 2 CYS H 142 CYS H 198 1555 1555 2.02
SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.07
SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.02
SSBOND 5 CYS V 26 CYS V 68 1555 1555 2.03
SSBOND 6 CYS V 51 CYS V 60 1555 4545 2.47
SSBOND 7 CYS V 57 CYS V 102 1555 1555 2.04
SSBOND 8 CYS V 61 CYS V 104 1555 1555 2.04
CISPEP 1 PHE H 148 PRO H 149 0 -5.36
CISPEP 2 GLU H 150 PRO H 151 0 0.19
CISPEP 3 SER L 7 PRO L 8 0 -0.94
CISPEP 4 THR L 94 PRO L 95 0 -6.04
CISPEP 5 TYR L 140 PRO L 141 0 2.32
CISPEP 6 LYS V 48 PRO V 49 0 0.11
SITE 1 AC1 6 GLN L 37 LYS L 39 PRO L 59 ARG L 61
SITE 2 AC1 6 GLU L 81 ASP L 82
CRYST1 100.600 197.978 77.650 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009940 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005051 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012878 0.00000
ATOM 1 N SER H 0 -37.927 -61.474 19.547 1.00 69.10 N
ATOM 2 CA SER H 0 -38.310 -60.292 18.715 1.00 71.53 C
ATOM 3 C SER H 0 -38.233 -60.590 17.204 1.00 71.93 C
ATOM 4 O SER H 0 -37.697 -61.629 16.785 1.00 71.95 O
ATOM 5 CB SER H 0 -37.448 -59.069 19.075 1.00 74.20 C
ATOM 6 OG SER H 0 -36.274 -58.986 18.276 1.00 75.19 O
ATOM 7 N GLU H 1 -38.756 -59.656 16.403 1.00 69.57 N
ATOM 8 CA GLU H 1 -39.004 -59.866 14.969 1.00 65.18 C
ATOM 9 C GLU H 1 -37.849 -59.370 14.072 1.00 56.27 C
ATOM 10 O GLU H 1 -37.116 -58.451 14.439 1.00 50.34 O
ATOM 11 CB GLU H 1 -40.306 -59.159 14.583 1.00 68.64 C
ATOM 12 CG GLU H 1 -40.935 -59.634 13.267 1.00 73.12 C
ATOM 13 CD GLU H 1 -41.403 -58.471 12.387 1.00 74.91 C
ATOM 14 OE1 GLU H 1 -40.980 -58.398 11.210 1.00 71.85 O
ATOM 15 OE2 GLU H 1 -42.186 -57.625 12.885 1.00 81.26 O
ATOM 16 N VAL H 2 -37.702 -59.997 12.902 1.00 51.20 N
ATOM 17 CA VAL H 2 -36.636 -59.662 11.953 1.00 49.61 C
ATOM 18 C VAL H 2 -36.801 -58.230 11.460 1.00 48.43 C
ATOM 19 O VAL H 2 -37.910 -57.787 11.176 1.00 47.04 O
ATOM 20 CB VAL H 2 -36.606 -60.600 10.708 1.00 45.35 C
ATOM 21 CG1 VAL H 2 -35.390 -60.270 9.819 1.00 42.45 C
ATOM 22 CG2 VAL H 2 -36.598 -62.068 11.100 1.00 38.88 C
ATOM 23 N GLN H 3 -35.692 -57.512 11.351 1.00 47.12 N
ATOM 24 CA GLN H 3 -35.744 -56.079 11.136 1.00 46.40 C
ATOM 25 C GLN H 3 -34.346 -55.579 10.786 1.00 46.20 C
ATOM 26 O GLN H 3 -33.351 -56.045 11.353 1.00 45.62 O
ATOM 27 CB GLN H 3 -36.234 -55.429 12.418 1.00 49.02 C
ATOM 28 CG GLN H 3 -36.826 -54.049 12.321 1.00 51.85 C
ATOM 29 CD GLN H 3 -37.059 -53.474 13.727 1.00 53.86 C
ATOM 30 OE1 GLN H 3 -36.668 -52.342 14.028 1.00 58.18 O
ATOM 31 NE2 GLN H 3 -37.647 -54.284 14.603 1.00 50.89 N
ATOM 32 N LEU H 4 -34.265 -54.649 9.841 1.00 45.54 N
ATOM 33 CA LEU H 4 -32.982 -54.070 9.443 1.00 44.24 C
ATOM 34 C LEU H 4 -33.120 -52.560 9.468 1.00 42.77 C
ATOM 35 O LEU H 4 -33.967 -52.017 8.797 1.00 47.00 O
ATOM 36 CB LEU H 4 -32.587 -54.551 8.042 1.00 45.46 C
ATOM 37 CG LEU H 4 -32.226 -56.026 7.777 1.00 44.52 C
ATOM 38 CD1 LEU H 4 -32.095 -56.298 6.257 1.00 41.33 C
ATOM 39 CD2 LEU H 4 -30.930 -56.416 8.499 1.00 41.38 C
ATOM 40 N VAL H 5 -32.306 -51.881 10.263 1.00 46.92 N
ATOM 41 CA VAL H 5 -32.404 -50.424 10.401 1.00 45.35 C
ATOM 42 C VAL H 5 -31.138 -49.737 9.882 1.00 46.67 C
ATOM 43 O VAL H 5 -30.075 -49.860 10.487 1.00 49.13 O
ATOM 44 CB VAL H 5 -32.632 -50.024 11.872 1.00 45.54 C
ATOM 45 CG1 VAL H 5 -32.749 -48.515 11.984 1.00 39.73 C
ATOM 46 CG2 VAL H 5 -33.883 -50.751 12.467 1.00 42.64 C
ATOM 47 N GLU H 6 -31.259 -49.035 8.752 1.00 49.55 N
ATOM 48 CA GLU H 6 -30.155 -48.259 8.187 1.00 46.76 C
ATOM 49 C GLU H 6 -29.964 -46.946 8.937 1.00 49.64 C
ATOM 50 O GLU H 6 -30.921 -46.376 9.470 1.00 49.92 O
ATOM 51 CB GLU H 6 -30.380 -47.931 6.716 1.00 48.05 C
ATOM 52 CG GLU H 6 -30.534 -49.127 5.807 1.00 48.69 C
ATOM 53 CD GLU H 6 -31.967 -49.426 5.489 1.00 53.90 C
ATOM 54 OE1 GLU H 6 -32.846 -49.089 6.314 1.00 60.10 O
ATOM 55 OE2 GLU H 6 -32.231 -50.014 4.422 1.00 55.43 O
ATOM 56 N SER H 7 -28.718 -46.474 8.970 1.00 50.24 N
ATOM 57 CA SER H 7 -28.400 -45.139 9.488 1.00 46.24 C
ATOM 58 C SER H 7 -27.106 -44.637 8.849 1.00 43.60 C
ATOM 59 O SER H 7 -26.437 -45.392 8.142 1.00 39.96 O
ATOM 60 CB SER H 7 -28.314 -45.134 11.020 1.00 44.18 C
ATOM 61 OG SER H 7 -27.207 -45.881 11.482 1.00 51.01 O
ATOM 62 N GLY H 8 -26.791 -43.356 9.066 1.00 43.05 N
ATOM 63 CA GLY H 8 -25.550 -42.757 8.573 1.00 42.22 C
ATOM 64 C GLY H 8 -25.597 -41.891 7.329 1.00 41.98 C
ATOM 65 O GLY H 8 -24.606 -41.229 6.991 1.00 45.71 O
ATOM 66 N GLY H 9 -26.731 -41.864 6.642 1.00 42.79 N
ATOM 67 CA GLY H 9 -26.839 -41.088 5.400 1.00 42.70 C
ATOM 68 C GLY H 9 -26.861 -39.587 5.644 1.00 48.54 C
ATOM 69 O GLY H 9 -27.009 -39.135 6.777 1.00 52.02 O
ATOM 70 N GLY H 10 -26.732 -38.813 4.572 1.00 46.08 N
ATOM 71 CA GLY H 10 -26.740 -37.366 4.671 1.00 40.48 C
ATOM 72 C GLY H 10 -25.993 -36.719 3.531 1.00 39.86 C
ATOM 73 O GLY H 10 -25.663 -37.375 2.553 1.00 42.61 O
ATOM 74 N LEU H 11 -25.733 -35.424 3.658 1.00 42.12 N
ATOM 75 CA LEU H 11 -25.093 -34.674 2.593 1.00 43.89 C
ATOM 76 C LEU H 11 -23.589 -34.910 2.638 1.00 48.14 C
ATOM 77 O LEU H 11 -23.019 -35.033 3.725 1.00 51.49 O
ATOM 78 CB LEU H 11 -25.395 -33.182 2.735 1.00 42.66 C
ATOM 79 CG LEU H 11 -24.663 -32.213 1.795 1.00 41.84 C
ATOM 80 CD1 LEU H 11 -25.148 -32.360 0.360 1.00 35.84 C
ATOM 81 CD2 LEU H 11 -24.837 -30.784 2.290 1.00 40.95 C
ATOM 82 N VAL H 12 -22.957 -34.973 1.462 1.00 46.46 N
ATOM 83 CA VAL H 12 -21.488 -35.066 1.363 1.00 46.21 C
ATOM 84 C VAL H 12 -20.940 -34.520 0.043 1.00 44.83 C
ATOM 85 O VAL H 12 -21.557 -34.646 -1.000 1.00 46.80 O
ATOM 86 CB VAL H 12 -20.987 -36.506 1.555 1.00 44.81 C
ATOM 87 CG1 VAL H 12 -21.680 -37.458 0.585 1.00 42.65 C
ATOM 88 CG2 VAL H 12 -19.478 -36.561 1.414 1.00 43.17 C
ATOM 89 N GLN H 13 -19.766 -33.913 0.110 1.00 48.02 N
ATOM 90 CA GLN H 13 -19.169 -33.272 -1.043 1.00 47.82 C
ATOM 91 C GLN H 13 -18.572 -34.274 -2.003 1.00 44.18 C
ATOM 92 O GLN H 13 -18.074 -35.307 -1.579 1.00 47.61 O
ATOM 93 CB GLN H 13 -18.085 -32.308 -0.580 1.00 47.90 C
ATOM 94 CG GLN H 13 -18.644 -31.181 0.256 1.00 51.29 C
ATOM 95 CD GLN H 13 -17.723 -29.994 0.304 1.00 54.56 C
ATOM 96 OE1 GLN H 13 -18.047 -28.920 -0.225 1.00 60.74 O
ATOM 97 NE2 GLN H 13 -16.549 -30.178 0.919 1.00 53.44 N
ATOM 98 N PRO H 14 -18.571 -33.951 -3.301 1.00 45.08 N
ATOM 99 CA PRO H 14 -17.879 -34.834 -4.253 1.00 47.56 C
ATOM 100 C PRO H 14 -16.426 -35.115 -3.828 1.00 45.07 C
ATOM 101 O PRO H 14 -15.749 -34.227 -3.301 1.00 38.25 O
ATOM 102 CB PRO H 14 -17.916 -34.048 -5.572 1.00 48.75 C
ATOM 103 CG PRO H 14 -19.002 -33.008 -5.403 1.00 47.40 C
ATOM 104 CD PRO H 14 -19.158 -32.755 -3.941 1.00 45.74 C
ATOM 105 N GLY H 15 -15.971 -36.351 -4.029 1.00 45.11 N
ATOM 106 CA GLY H 15 -14.642 -36.773 -3.578 1.00 45.26 C
ATOM 107 C GLY H 15 -14.603 -37.185 -2.111 1.00 46.93 C
ATOM 108 O GLY H 15 -13.604 -37.733 -1.644 1.00 45.40 O
ATOM 109 N GLY H 16 -15.702 -36.943 -1.395 1.00 49.15 N
ATOM 110 CA GLY H 16 -15.786 -37.185 0.037 1.00 47.95 C
ATOM 111 C GLY H 16 -16.172 -38.604 0.401 1.00 47.57 C
ATOM 112 O GLY H 16 -16.458 -39.428 -0.460 1.00 47.48 O
ATOM 113 N SER H 17 -16.192 -38.860 1.704 1.00 51.04 N
ATOM 114 CA SER H 17 -16.388 -40.186 2.276 1.00 49.94 C
ATOM 115 C SER H 17 -17.588 -40.185 3.189 1.00 48.51 C
ATOM 116 O SER H 17 -17.974 -39.151 3.731 1.00 48.56 O
ATOM 117 CB SER H 17 -15.160 -40.604 3.097 1.00 53.91 C
ATOM 118 OG SER H 17 -14.231 -41.363 2.332 1.00 57.62 O
ATOM 119 N LEU H 18 -18.155 -41.365 3.386 1.00 50.62 N
ATOM 120 CA LEU H 18 -19.324 -41.529 4.228 1.00 48.68 C
ATOM 121 C LEU H 18 -19.460 -43.006 4.531 1.00 50.18 C
ATOM 122 O LEU H 18 -19.051 -43.850 3.735 1.00 50.03 O
ATOM 123 CB LEU H 18 -20.572 -41.049 3.491 1.00 50.69 C
ATOM 124 CG LEU H 18 -21.723 -40.672 4.410 1.00 54.39 C
ATOM 125 CD1 LEU H 18 -21.363 -39.374 5.149 1.00 55.58 C
ATOM 126 CD2 LEU H 18 -23.036 -40.527 3.641 1.00 51.69 C
ATOM 127 N ARG H 19 -20.065 -43.314 5.667 1.00 51.58 N
ATOM 128 CA ARG H 19 -20.182 -44.679 6.140 1.00 48.41 C
ATOM 129 C ARG H 19 -21.591 -44.953 6.602 1.00 41.62 C
ATOM 130 O ARG H 19 -22.057 -44.321 7.533 1.00 40.53 O
ATOM 131 CB ARG H 19 -19.220 -44.883 7.308 1.00 52.42 C
ATOM 132 CG ARG H 19 -19.060 -46.326 7.778 1.00 53.20 C
ATOM 133 CD ARG H 19 -18.854 -46.340 9.272 1.00 56.48 C
ATOM 134 NE ARG H 19 -18.262 -47.578 9.753 1.00 58.18 N
ATOM 135 CZ ARG H 19 -18.216 -47.941 11.035 1.00 60.91 C
ATOM 136 NH1 ARG H 19 -18.748 -47.170 11.986 1.00 59.05 N
ATOM 137 NH2 ARG H 19 -17.646 -49.098 11.366 1.00 61.68 N
ATOM 138 N LEU H 20 -22.256 -45.922 5.973 1.00 45.38 N
ATOM 139 CA LEU H 20 -23.602 -46.317 6.373 1.00 43.97 C
ATOM 140 C LEU H 20 -23.565 -47.558 7.248 1.00 47.58 C
ATOM 141 O LEU H 20 -22.693 -48.409 7.083 1.00 45.27 O
ATOM 142 CB LEU H 20 -24.461 -46.581 5.145 1.00 40.18 C
ATOM 143 CG LEU H 20 -24.392 -45.511 4.051 1.00 40.45 C
ATOM 144 CD1 LEU H 20 -25.486 -45.755 2.991 1.00 37.03 C
ATOM 145 CD2 LEU H 20 -24.506 -44.102 4.647 1.00 37.42 C
ATOM 146 N SER H 21 -24.526 -47.644 8.169 1.00 49.80 N
ATOM 147 CA SER H 21 -24.688 -48.784 9.079 1.00 44.98 C
ATOM 148 C SER H 21 -26.031 -49.458 8.835 1.00 47.26 C
ATOM 149 O SER H 21 -26.987 -48.822 8.385 1.00 47.11 O
ATOM 150 CB SER H 21 -24.645 -48.327 10.536 1.00 38.57 C
ATOM 151 OG SER H 21 -23.399 -47.758 10.846 1.00 42.88 O
ATOM 152 N CYS H 22 -26.100 -50.744 9.156 1.00 47.91 N
ATOM 153 CA CYS H 22 -27.329 -51.495 9.044 1.00 46.37 C
ATOM 154 C CYS H 22 -27.452 -52.426 10.243 1.00 46.70 C
ATOM 155 O CYS H 22 -26.837 -53.487 10.268 1.00 47.37 O
ATOM 156 CB CYS H 22 -27.350 -52.299 7.744 1.00 48.43 C
ATOM 157 SG CYS H 22 -28.847 -53.307 7.572 1.00 58.24 S
ATOM 158 N ALA H 23 -28.245 -52.022 11.234 1.00 44.93 N
ATOM 159 CA ALA H 23 -28.450 -52.829 12.436 1.00 42.12 C
ATOM 160 C ALA H 23 -29.483 -53.942 12.198 1.00 38.03 C
ATOM 161 O ALA H 23 -30.644 -53.661 11.928 1.00 43.17 O
ATOM 162 CB ALA H 23 -28.880 -51.937 13.602 1.00 34.03 C
ATOM 163 N ALA H 24 -29.053 -55.194 12.313 1.00 36.57 N
ATOM 164 CA ALA H 24 -29.930 -56.358 12.139 1.00 37.86 C
ATOM 165 C ALA H 24 -30.510 -56.767 13.475 1.00 34.95 C
ATOM 166 O ALA H 24 -29.837 -56.670 14.471 1.00 33.48 O
ATOM 167 CB ALA H 24 -29.158 -57.519 11.545 1.00 39.59 C
ATOM 168 N SER H 25 -31.757 -57.231 13.473 1.00 37.91 N
ATOM 169 CA SER H 25 -32.459 -57.687 14.680 1.00 37.76 C
ATOM 170 C SER H 25 -33.275 -58.913 14.362 1.00 38.61 C
ATOM 171 O SER H 25 -33.789 -59.028 13.246 1.00 40.55 O
ATOM 172 CB SER H 25 -33.447 -56.637 15.164 1.00 38.24 C
ATOM 173 OG SER H 25 -32.782 -55.561 15.769 1.00 41.58 O
ATOM 174 N GLY H 26 -33.435 -59.787 15.359 1.00 37.52 N
ATOM 175 CA GLY H 26 -34.280 -60.979 15.247 1.00 37.05 C
ATOM 176 C GLY H 26 -33.698 -62.138 14.450 1.00 36.12 C
ATOM 177 O GLY H 26 -34.398 -63.098 14.149 1.00 38.81 O
ATOM 178 N PHE H 27 -32.430 -62.035 14.078 1.00 39.67 N
ATOM 179 CA PHE H 27 -31.681 -63.150 13.494 1.00 43.06 C
ATOM 180 C PHE H 27 -30.193 -62.793 13.595 1.00 44.90 C
ATOM 181 O PHE H 27 -29.859 -61.650 13.890 1.00 43.41 O
ATOM 182 CB PHE H 27 -32.080 -63.386 12.035 1.00 41.10 C
ATOM 183 CG PHE H 27 -31.625 -62.304 11.104 1.00 43.33 C
ATOM 184 CD1 PHE H 27 -30.612 -62.542 10.168 1.00 42.93 C
ATOM 185 CD2 PHE H 27 -32.198 -61.034 11.162 1.00 42.47 C
ATOM 186 CE1 PHE H 27 -30.189 -61.536 9.296 1.00 41.03 C
ATOM 187 CE2 PHE H 27 -31.773 -60.023 10.296 1.00 42.89 C
ATOM 188 CZ PHE H 27 -30.764 -60.276 9.363 1.00 40.93 C
ATOM 189 N ASN H 28 -29.311 -63.763 13.375 1.00 46.65 N
ATOM 190 CA ASN H 28 -27.878 -63.498 13.373 1.00 48.24 C
ATOM 191 C ASN H 28 -27.425 -63.337 11.946 1.00 44.49 C
ATOM 192 O ASN H 28 -27.671 -64.213 11.123 1.00 37.07 O
ATOM 193 CB ASN H 28 -27.112 -64.624 14.065 1.00 56.86 C
ATOM 194 CG ASN H 28 -27.437 -64.709 15.558 1.00 66.77 C
ATOM 195 OD1 ASN H 28 -27.278 -63.731 16.297 1.00 72.77 O
ATOM 196 ND2 ASN H 28 -27.915 -65.876 16.003 1.00 70.06 N
ATOM 197 N ILE H 29 -26.778 -62.212 11.647 1.00 43.94 N
ATOM 198 CA ILE H 29 -26.319 -61.957 10.283 1.00 44.03 C
ATOM 199 C ILE H 29 -25.333 -63.010 9.787 1.00 43.31 C
ATOM 200 O ILE H 29 -25.170 -63.161 8.588 1.00 42.67 O
ATOM 201 CB ILE H 29 -25.743 -60.544 10.083 1.00 41.98 C
ATOM 202 CG1 ILE H 29 -24.518 -60.288 10.970 1.00 42.48 C
ATOM 203 CG2 ILE H 29 -26.819 -59.491 10.329 1.00 39.47 C
ATOM 204 CD1 ILE H 29 -23.919 -58.905 10.718 1.00 41.05 C
ATOM 205 N LYS H 30 -24.723 -63.764 10.702 1.00 47.57 N
ATOM 206 CA LYS H 30 -23.885 -64.934 10.350 1.00 50.45 C
ATOM 207 C LYS H 30 -24.588 -65.980 9.472 1.00 46.58 C
ATOM 208 O LYS H 30 -23.932 -66.718 8.750 1.00 49.47 O
ATOM 209 CB LYS H 30 -23.360 -65.636 11.624 1.00 53.57 C
ATOM 210 CG LYS H 30 -22.264 -64.867 12.360 1.00 58.23 C
ATOM 211 CD LYS H 30 -21.743 -65.607 13.600 1.00 57.76 C
ATOM 212 CE LYS H 30 -20.679 -66.674 13.254 1.00 60.63 C
ATOM 213 NZ LYS H 30 -19.866 -67.129 14.444 1.00 61.42 N
ATOM 214 N ASP H 31 -25.911 -66.053 9.548 1.00 48.22 N
ATOM 215 CA ASP H 31 -26.662 -67.125 8.890 1.00 49.78 C
ATOM 216 C ASP H 31 -26.904 -66.876 7.409 1.00 49.04 C
ATOM 217 O ASP H 31 -27.352 -67.776 6.699 1.00 49.13 O
ATOM 218 CB ASP H 31 -28.003 -67.364 9.604 1.00 47.31 C
ATOM 219 CG ASP H 31 -27.830 -67.940 11.007 1.00 52.17 C
ATOM 220 OD1 ASP H 31 -26.764 -68.527 11.311 1.00 48.35 O
ATOM 221 OD2 ASP H 31 -28.778 -67.799 11.811 1.00 55.74 O
ATOM 222 N THR H 32 -26.606 -65.670 6.935 1.00 50.56 N
ATOM 223 CA THR H 32 -26.962 -65.295 5.576 1.00 49.16 C
ATOM 224 C THR H 32 -26.083 -64.186 5.004 1.00 45.86 C
ATOM 225 O THR H 32 -25.113 -63.792 5.626 1.00 51.99 O
ATOM 226 CB THR H 32 -28.423 -64.838 5.533 1.00 48.30 C
ATOM 227 OG1 THR H 32 -28.854 -64.753 4.159 1.00 51.35 O
ATOM 228 CG2 THR H 32 -28.563 -63.475 6.246 1.00 42.98 C
ATOM 229 N TYR H 33 -26.438 -63.701 3.811 1.00 44.42 N
ATOM 230 CA TYR H 33 -25.766 -62.570 3.172 1.00 44.79 C
ATOM 231 C TYR H 33 -26.547 -61.299 3.429 1.00 44.52 C
ATOM 232 O TYR H 33 -27.768 -61.313 3.451 1.00 44.01 O
ATOM 233 CB TYR H 33 -25.648 -62.762 1.658 1.00 45.56 C
ATOM 234 CG TYR H 33 -24.425 -63.536 1.197 1.00 47.47 C
ATOM 235 CD1 TYR H 33 -24.387 -64.920 1.249 1.00 46.56 C
ATOM 236 CD2 TYR H 33 -23.320 -62.876 0.663 1.00 47.06 C
ATOM 237 CE1 TYR H 33 -23.263 -65.627 0.806 1.00 47.42 C
ATOM 238 CE2 TYR H 33 -22.196 -63.564 0.220 1.00 45.32 C
ATOM 239 CZ TYR H 33 -22.159 -64.943 0.294 1.00 49.10 C
ATOM 240 OH TYR H 33 -21.019 -65.646 -0.137 1.00 48.57 O
ATOM 241 N ILE H 34 -25.820 -60.204 3.612 1.00 46.50 N
ATOM 242 CA ILE H 34 -26.384 -58.868 3.710 1.00 45.24 C
ATOM 243 C ILE H 34 -25.958 -58.104 2.446 1.00 43.22 C
ATOM 244 O ILE H 34 -24.824 -58.199 2.012 1.00 46.29 O
ATOM 245 CB ILE H 34 -25.851 -58.134 4.977 1.00 44.09 C
ATOM 246 CG1 ILE H 34 -26.169 -58.935 6.253 1.00 46.27 C
ATOM 247 CG2 ILE H 34 -26.408 -56.725 5.087 1.00 45.88 C
ATOM 248 CD1 ILE H 34 -27.666 -59.211 6.524 1.00 41.89 C
ATOM 249 N HIS H 35 -26.874 -57.339 1.882 1.00 42.12 N
ATOM 250 CA HIS H 35 -26.627 -56.576 0.683 1.00 44.91 C
ATOM 251 C HIS H 35 -26.892 -55.110 0.908 1.00 44.00 C
ATOM 252 O HIS H 35 -27.674 -54.736 1.757 1.00 45.73 O
ATOM 253 CB HIS H 35 -27.598 -56.990 -0.435 1.00 46.00 C
ATOM 254 CG HIS H 35 -27.678 -58.459 -0.666 1.00 43.43 C
ATOM 255 ND1 HIS H 35 -26.938 -59.092 -1.634 1.00 39.96 N
ATOM 256 CD2 HIS H 35 -28.414 -59.421 -0.062 1.00 47.61 C
ATOM 257 CE1 HIS H 35 -27.209 -60.386 -1.617 1.00 45.15 C
ATOM 258 NE2 HIS H 35 -28.108 -60.610 -0.677 1.00 46.56 N
ATOM 259 N TRP H 36 -26.269 -54.288 0.084 1.00 49.65 N
ATOM 260 CA TRP H 36 -26.712 -52.929 -0.098 1.00 50.50 C
ATOM 261 C TRP H 36 -27.245 -52.837 -1.503 1.00 49.74 C
ATOM 262 O TRP H 36 -26.605 -53.308 -2.442 1.00 49.33 O
ATOM 263 CB TRP H 36 -25.574 -51.947 0.119 1.00 48.96 C
ATOM 264 CG TRP H 36 -25.198 -51.863 1.553 1.00 48.26 C
ATOM 265 CD1 TRP H 36 -24.231 -52.580 2.199 1.00 50.52 C
ATOM 266 CD2 TRP H 36 -25.783 -51.019 2.527 1.00 44.74 C
ATOM 267 NE1 TRP H 36 -24.166 -52.214 3.526 1.00 47.95 N
ATOM 268 CE2 TRP H 36 -25.119 -51.263 3.753 1.00 44.78 C
ATOM 269 CE3 TRP H 36 -26.784 -50.058 2.482 1.00 47.66 C
ATOM 270 CZ2 TRP H 36 -25.433 -50.590 4.912 1.00 47.96 C
ATOM 271 CZ3 TRP H 36 -27.110 -49.395 3.646 1.00 50.56 C
ATOM 272 CH2 TRP H 36 -26.428 -49.656 4.845 1.00 50.29 C
ATOM 273 N VAL H 37 -28.441 -52.267 -1.617 1.00 49.52 N
ATOM 274 CA VAL H 37 -29.087 -51.990 -2.897 1.00 47.75 C
ATOM 275 C VAL H 37 -29.575 -50.544 -2.891 1.00 47.18 C
ATOM 276 O VAL H 37 -30.187 -50.103 -1.916 1.00 45.21 O
ATOM 277 CB VAL H 37 -30.282 -52.889 -3.085 1.00 44.60 C
ATOM 278 CG1 VAL H 37 -30.967 -52.555 -4.372 1.00 40.23 C
ATOM 279 CG2 VAL H 37 -29.835 -54.342 -2.993 1.00 43.77 C
ATOM 280 N ARG H 38 -29.312 -49.812 -3.968 1.00 42.23 N
ATOM 281 CA ARG H 38 -29.600 -48.392 -3.975 1.00 42.83 C
ATOM 282 C ARG H 38 -30.494 -47.993 -5.125 1.00 44.68 C
ATOM 283 O ARG H 38 -30.611 -48.698 -6.124 1.00 49.39 O
ATOM 284 CB ARG H 38 -28.300 -47.590 -4.029 1.00 43.45 C
ATOM 285 CG ARG H 38 -27.709 -47.460 -5.409 1.00 40.33 C
ATOM 286 CD ARG H 38 -26.330 -46.834 -5.387 1.00 42.65 C
ATOM 287 NE ARG H 38 -25.722 -46.986 -6.702 1.00 44.78 N
ATOM 288 CZ ARG H 38 -24.591 -46.422 -7.102 1.00 46.76 C
ATOM 289 NH1 ARG H 38 -23.861 -45.673 -6.290 1.00 48.65 N
ATOM 290 NH2 ARG H 38 -24.177 -46.629 -8.338 1.00 50.05 N
ATOM 291 N GLN H 39 -31.093 -46.825 -4.980 1.00 45.61 N
ATOM 292 CA GLN H 39 -32.053 -46.308 -5.939 1.00 44.89 C
ATOM 293 C GLN H 39 -31.857 -44.797 -6.077 1.00 43.63 C
ATOM 294 O GLN H 39 -32.133 -44.036 -5.151 1.00 37.62 O
ATOM 295 CB GLN H 39 -33.475 -46.612 -5.468 1.00 41.68 C
ATOM 296 CG GLN H 39 -34.590 -46.053 -6.351 1.00 42.17 C
ATOM 297 CD GLN H 39 -35.930 -46.664 -5.998 1.00 42.97 C
ATOM 298 OE1 GLN H 39 -36.340 -46.619 -4.846 1.00 47.93 O
ATOM 299 NE2 GLN H 39 -36.598 -47.272 -6.976 1.00 41.16 N
ATOM 300 N ALA H 40 -31.367 -44.392 -7.239 1.00 42.77 N
ATOM 301 CA ALA H 40 -31.226 -42.992 -7.577 1.00 46.13 C
ATOM 302 C ALA H 40 -32.633 -42.421 -7.783 1.00 49.61 C
ATOM 303 O ALA H 40 -33.542 -43.166 -8.114 1.00 44.62 O
ATOM 304 CB ALA H 40 -30.382 -42.842 -8.855 1.00 34.93 C
ATOM 305 N PRO H 41 -32.807 -41.102 -7.588 1.00 55.43 N
ATOM 306 CA PRO H 41 -34.117 -40.444 -7.688 1.00 52.93 C
ATOM 307 C PRO H 41 -34.829 -40.740 -8.996 1.00 54.54 C
ATOM 308 O PRO H 41 -34.267 -40.513 -10.073 1.00 53.54 O
ATOM 309 CB PRO H 41 -33.773 -38.953 -7.607 1.00 56.13 C
ATOM 310 CG PRO H 41 -32.486 -38.901 -6.853 1.00 57.63 C
ATOM 311 CD PRO H 41 -31.734 -40.145 -7.245 1.00 57.03 C
ATOM 312 N GLY H 42 -36.056 -41.255 -8.884 1.00 53.62 N
ATOM 313 CA GLY H 42 -36.863 -41.634 -10.039 1.00 49.51 C
ATOM 314 C GLY H 42 -36.387 -42.816 -10.876 1.00 48.83 C
ATOM 315 O GLY H 42 -36.935 -43.066 -11.945 1.00 52.46 O
ATOM 316 N LYS H 43 -35.377 -43.548 -10.422 1.00 49.60 N
ATOM 317 CA LYS H 43 -34.809 -44.643 -11.216 1.00 51.02 C
ATOM 318 C LYS H 43 -35.109 -45.964 -10.525 1.00 46.44 C
ATOM 319 O LYS H 43 -35.881 -45.995 -9.564 1.00 46.30 O
ATOM 320 CB LYS H 43 -33.289 -44.487 -11.399 1.00 59.14 C
ATOM 321 CG LYS H 43 -32.790 -43.074 -11.662 1.00 62.24 C
ATOM 322 CD LYS H 43 -33.524 -42.400 -12.809 1.00 65.66 C
ATOM 323 CE LYS H 43 -32.909 -41.033 -13.149 1.00 65.64 C
ATOM 324 NZ LYS H 43 -33.763 -40.265 -14.113 1.00 63.40 N
ATOM 325 N GLY H 44 -34.497 -47.039 -11.023 1.00 43.57 N
ATOM 326 CA GLY H 44 -34.729 -48.399 -10.526 1.00 44.83 C
ATOM 327 C GLY H 44 -33.815 -48.813 -9.379 1.00 45.51 C
ATOM 328 O GLY H 44 -33.251 -47.976 -8.691 1.00 47.03 O
ATOM 329 N LEU H 45 -33.698 -50.120 -9.170 1.00 46.62 N
ATOM 330 CA LEU H 45 -33.002 -50.688 -8.029 1.00 42.35 C
ATOM 331 C LEU H 45 -31.717 -51.284 -8.563 1.00 45.85 C
ATOM 332 O LEU H 45 -31.746 -52.027 -9.544 1.00 42.07 O
ATOM 333 CB LEU H 45 -33.848 -51.798 -7.387 1.00 41.48 C
ATOM 334 CG LEU H 45 -35.179 -51.394 -6.738 1.00 39.20 C
ATOM 335 CD1 LEU H 45 -36.161 -52.579 -6.653 1.00 36.10 C
ATOM 336 CD2 LEU H 45 -34.925 -50.770 -5.352 1.00 32.74 C
ATOM 337 N GLU H 46 -30.601 -50.963 -7.912 1.00 47.55 N
ATOM 338 CA GLU H 46 -29.275 -51.343 -8.378 1.00 46.78 C
ATOM 339 C GLU H 46 -28.523 -51.996 -7.218 1.00 48.07 C
ATOM 340 O GLU H 46 -28.185 -51.354 -6.229 1.00 53.74 O
ATOM 341 CB GLU H 46 -28.500 -50.114 -8.903 1.00 46.50 C
ATOM 342 CG GLU H 46 -27.071 -50.452 -9.426 1.00 48.51 C
ATOM 343 CD GLU H 46 -26.150 -49.243 -9.684 1.00 48.67 C
ATOM 344 OE1 GLU H 46 -26.407 -48.104 -9.196 1.00 45.81 O
ATOM 345 OE2 GLU H 46 -25.141 -49.453 -10.391 1.00 49.38 O
ATOM 346 N TRP H 47 -28.280 -53.285 -7.343 1.00 48.87 N
ATOM 347 CA TRP H 47 -27.508 -54.008 -6.356 1.00 48.10 C
ATOM 348 C TRP H 47 -26.084 -53.469 -6.432 1.00 49.55 C
ATOM 349 O TRP H 47 -25.559 -53.314 -7.546 1.00 49.40 O
ATOM 350 CB TRP H 47 -27.556 -55.523 -6.650 1.00 46.57 C
ATOM 351 CG TRP H 47 -26.678 -56.298 -5.766 1.00 47.39 C
ATOM 352 CD1 TRP H 47 -26.988 -56.812 -4.550 1.00 47.14 C
ATOM 353 CD2 TRP H 47 -25.312 -56.614 -6.000 1.00 47.63 C
ATOM 354 NE1 TRP H 47 -25.908 -57.455 -4.024 1.00 45.58 N
ATOM 355 CE2 TRP H 47 -24.859 -57.339 -4.890 1.00 45.99 C
ATOM 356 CE3 TRP H 47 -24.431 -56.363 -7.050 1.00 47.75 C
ATOM 357 CZ2 TRP H 47 -23.562 -57.819 -4.792 1.00 49.59 C
ATOM 358 CZ3 TRP H 47 -23.145 -56.841 -6.961 1.00 48.59 C
ATOM 359 CH2 TRP H 47 -22.717 -57.561 -5.834 1.00 49.79 C
ATOM 360 N VAL H 48 -25.457 -53.171 -5.283 1.00 43.69 N
ATOM 361 CA VAL H 48 -24.052 -52.732 -5.324 1.00 44.55 C
ATOM 362 C VAL H 48 -23.038 -53.563 -4.553 1.00 43.26 C
ATOM 363 O VAL H 48 -21.896 -53.625 -4.966 1.00 47.93 O
ATOM 364 CB VAL H 48 -23.874 -51.257 -4.926 1.00 49.14 C
ATOM 365 CG1 VAL H 48 -24.515 -50.365 -5.983 1.00 50.29 C
ATOM 366 CG2 VAL H 48 -24.425 -50.983 -3.539 1.00 43.91 C